RESUMEN
The interaction of Inga laurina Kunitz inhibitor with insect trypsins is an example of protein-protein interaction with potential application for the pest control. However, the crop field application of proteins as inhibitors is limited due to high production cost, the large molecular size and low environmental stability. The use of mimetic peptides that have molecular features associated with the protein inhibitor can result in a product with lower cost and higher efficiency for the agricultural application. Here, we designed mimetic peptides deriving from globular domains of ILTI that are predicted to interact with trypsin enzymes of Lepidoptera pest. Two linear peptides were identified and synthetized from the interface of interaction between trypsin-ILTI complexes. These peptides were derived due to its high-energy contribution for the biding affinity between the enzyme-protein inhibitor. The peptides showed structural stability, propensity to adopt the bound conformation also without the context of the protein, inhibitory activity of digestive trypsins and toxic effects on the S. cosmioides, indicating that they can be used as potential inhibitor for pest control.